4eti: Difference between revisions
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New page: '''Unreleased structure''' The entry 4eti is ON HOLD Authors: Cao, X.F. Description: Crystal Structure of YwlE from Bacillus subtilis |
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==Crystal Structure of YwlE from Bacillus subtilis== | |||
<StructureSection load='4eti' size='340' side='right'caption='[[4eti]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4eti]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ETI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ETI FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eti OCA], [https://pdbe.org/4eti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eti RCSB], [https://www.ebi.ac.uk/pdbsum/4eti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eti ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAP_BACSU PAP_BACSU] Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.<ref>PMID:22517742</ref> <ref>PMID:23770242</ref> <ref>PMID:24263382</ref> | |||
==See Also== | |||
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | |||
[[Category: Large Structures]] | |||
[[Category: Brostromer E]] | |||
[[Category: Cao XF]] | |||
[[Category: Liu XY]] | |||
[[Category: Su XD]] | |||
